Protein dynamics of resurrected ancestral enzymes studied by crystallography

Adaptation of organisms to environmental niches is a hallmark of evolution. One prevalent example is that of thermal adaptation, where in two descendants evolve at
different temperature extremes. How dynamical changes due to adaptive mutations are allosterically propagated to the active site, to modulate activity, in different
thermally adapted enzyme is not known. To address this question we analyze the properties of resurrected ancestral enzymes engaged in a thermal adaptation route
we recapitulated. We will solve the crystal structure several billions-years old enzymes and we will explore their dynamical properties following X-rays data
collection at various temperature. We expect describing the evolutionary-driven reorganization of contacts network that are required to conserve appropriate
conformational stability and efficient functional dynamics during the early steps of an enzyme adaptive process.